Source:http://linkedlifedata.com/resource/pubmed/id/15589995
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2004-12-13
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pubmed:abstractText |
Ca2+ affinity of cardiac troponin C (TnC) is regulated by the active cross-bridges (downstream-dependent mechanism). In the present study, we showed one of the methods to evaluate the downstream-dependent change in the Ca2+ affinity of TnC during contraction using the aequorin-injected ferret papillary muscle. For this purpose, the tension-dependent change in the extra-Ca2+ (a transient increase in the intracellular Ca2+ concentration ([Ca2+]i) in response to a quick length reduction) was measured under various conditions. We examined whether the regression line between the magnitude of tension reduction and the magnitude of the normalized extra-Ca2+ (the extra-Ca2+ was divided by [Ca2+]i immediately before length change) (the normalized extra-Ca2+-tension relation) in twitch contraction can be used for the estimation of the downstream-dependent change in the Ca2+ affinity of TnC. The normalized extra-Ca2+-tension relation became shallow by EMD 57033 (EMD) (one of the Ca2+ sensitizers) and by an increase in Ca2+ concentration in the solution ([Ca2+]o) in a concentration-dependent manner. However, 2,3-butanedione monoxime (BDM) (one of the desensitizers) antagonized the effects of EMD and higher [Ca2+]o in a concentration-dependent manner. These effects of EMD and BDM were also observed in the normalized extra-Ca2+-tension relation in tetanic contraction. The normalized extra-Ca2+-tension relation became steep by shortening the initial muscle length before contraction in tetanic contraction. Length-tension relation in twitch contraction was significantly shifted upward by higher [Ca2+]o and EMD, but BDM showed the opposite effects on them in a concentration-dependent manner. Thus, the downstream-dependent change in the Ca2+ affinity of TnC which physiologically functions in intact cardiac muscle can be evaluated using the normalized extra-Ca2+-tension relation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aequorin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Diacetyl,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin C,
http://linkedlifedata.com/resource/pubmed/chemical/diacetylmonoxime
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0143-4160
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
153-62
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15589995-Aequorin,
pubmed-meshheading:15589995-Animals,
pubmed-meshheading:15589995-Calcium,
pubmed-meshheading:15589995-Diacetyl,
pubmed-meshheading:15589995-Ferrets,
pubmed-meshheading:15589995-Heart Ventricles,
pubmed-meshheading:15589995-Luminescent Agents,
pubmed-meshheading:15589995-Male,
pubmed-meshheading:15589995-Muscle Contraction,
pubmed-meshheading:15589995-Troponin C
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pubmed:year |
2005
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pubmed:articleTitle |
Evaluation of the cross-bridge-dependent change in the Ca2+ affinity of troponin C in aequorin-injected ferret ventricular muscles.
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pubmed:affiliation |
Department of Internal Medicine, The Jikei University School of Medicine, 3-25-8 Nishi-Shimbashi, Minato-ku, Tokyo 105-8461, Japan. ishikawa@jikei.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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